A de novo designed monomeric, compact three helix bundle protein on a carbohydrate template
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A de novo designed monomeric, compact three helix bundle protein on a carbohydrate template. / Malik, Leila; Nygård, Jesper; Christensen, Niels Johan; Madsen, Charlotte Stahl; Rösner, Heike Ilona; Kragelund, Birthe Brandt; Høiberg-Nielsen, Rasmus; Streicher, Werner; Arleth, Lise; Thulstrup, Peter Waaben; Jensen, Knud Jørgen.
In: ChemBioChem, Vol. 16, No. 13, 2015, p. 1905-1918.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - A de novo designed monomeric, compact three helix bundle protein on a carbohydrate template
AU - Malik, Leila
AU - Nygård, Jesper
AU - Christensen, Niels Johan
AU - Madsen, Charlotte Stahl
AU - Rösner, Heike Ilona
AU - Kragelund, Birthe Brandt
AU - Høiberg-Nielsen, Rasmus
AU - Streicher, Werner
AU - Arleth, Lise
AU - Thulstrup, Peter Waaben
AU - Jensen, Knud Jørgen
N1 - © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
PY - 2015
Y1 - 2015
N2 - De novo design and chemical synthesis of proteins and of other artificial structures, which mimic them, is a central strategy for understanding protein folding and for accessing proteins with novel functions. We have previously described carbohydrates as templates for the assembly of artificial proteins, so called carboproteins. The hypothesis is that the template pre-organizes the secondary structure elements and directs the formation of a tertiary structure, thus achieving structural economy in the combination of peptide, linker, and template. We speculate that the structural information from the template could facilitate protein folding. Here we report the design and synthesis of 3-helix bundle carboproteins on deoxy-hexopyranosides. The carboproteins were analyzed by CD, AUC, SAXS, and NMR, which revealed the formation of the first compact, and folded monomeric carboprotein distinctly different to a molten globule.
AB - De novo design and chemical synthesis of proteins and of other artificial structures, which mimic them, is a central strategy for understanding protein folding and for accessing proteins with novel functions. We have previously described carbohydrates as templates for the assembly of artificial proteins, so called carboproteins. The hypothesis is that the template pre-organizes the secondary structure elements and directs the formation of a tertiary structure, thus achieving structural economy in the combination of peptide, linker, and template. We speculate that the structural information from the template could facilitate protein folding. Here we report the design and synthesis of 3-helix bundle carboproteins on deoxy-hexopyranosides. The carboproteins were analyzed by CD, AUC, SAXS, and NMR, which revealed the formation of the first compact, and folded monomeric carboprotein distinctly different to a molten globule.
U2 - 10.1002/cbic.201500285
DO - 10.1002/cbic.201500285
M3 - Journal article
C2 - 26147795
VL - 16
SP - 1905
EP - 1918
JO - ChemBioChem
JF - ChemBioChem
SN - 1439-4227
IS - 13
ER -
ID: 141044060